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Item No. 40874

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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWRift Valley fever virus (RVFV) is a single-stranded negative-sense RNA virus, member of the Phlebovirus genus, and mosquito-transmitted pathogen endemic to sub-Saharan Africa and the Arabian peninsula.1,2,3 The tripartite RNA genome of RVFV is composed of three segments: L, which encodes L protein, a single-polypeptide viral RNA-dependent RNA polymerase (RdRp), M, which encodes a single open reading frame (ORF) that produces the envelope glycoproteins Gn and Gc and non-structural proteins NSm and Gn/NSm fusion protein, and S, which is ambisense, encoding the nucleoprotein N in the genomic sense orientation and the non-structural protein and major virulence factor NSs in the antigenomic orientation.3,2 RVFV glycoprotein Gc is a class II membrane fusion protein that mediates viral entry and is composed of three domains: domain I, which is a 10-stranded β-barrel that organizes the glycoprotein structure, β-stranded domain II, and IgC-like domain III.4 Cayman’s RVFV Glycoprotein Gc (Strain MP12) (recombinant) protein consists of 459 amino acids and has a calculated molecular weight of 50.1 kDa.
WARNING This product is not for human or veterinary use.
1. Structure of Rift Valley Fever Virus RNA-
2. Rift Valley fever virus structural and nonstructural proteins: recombinant protein expression and immunoreactivity against antisera from sheep. Vector Borne Zoonotic Dis. 13(9), 619-629 (2013).
3. Molecular aspects of Rift Valley fever virus and the emergence of reassortants. Virus Genes 55(1), (2019).
4. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl. Acad. Sci. USA 110(5), 1696-1701 (2013).